Expression of heat shock proteins in squamous cell carcinoma of the tongue: an immunohistochemical study.
Twenty-four specimens of squamous cell carcinoma of the tongue were immunostained for heat shock proteins (HSPs) to reveal differences in stainability among normal epithelium, dysplasia and carcinoma and to clarify the prognostic significance of HSPs in comparison with survival period, clinical stage, lymph node metastasis, histological grade, and p53 immunostaining. Normal epithelium was positively stained in the suprabasal layer for HSP60 and HSP70, but was negative for HSP27 and HSP90. Dysplastic lesions were positive for HSP27, HSP70 and HSP90, but stained variously for HSP60. In squamous cell carcinoma, the cytoplasm of suprabasal tumor cells was often positive for HSP27 and HSP90 (18/24, 17/24, respectively). Although HSP immunohistochemistry has revealed changes in HSP expression during tumorigenesis of squamous epithelium of the tongue, there was no correlation between HSP staining and survival period, stage, lymph node metastasis, histological grade or p53 immunostaining.
Ito
T
T
Department of Pathology, Yokohama City University School of Medicine, Yokohama, Japan.
Kawabe
R
R
Kurasono
Y
Y
Hara
M
M
Kitamura
H
H
Fujita
K
K
Kanisawa
M
M
D002294:Carcinoma, Squamous Cell / Q000378:metabolism* / Q000473:pathology; D015972:Gene Expression Regulation, Neoplastic; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006801:Humans; D007150:Immunohistochemistry; D009061:Mouth Mucosa / Q000737:chemistry / Q000473:pathology; D009367:Neoplasm Staging; D011379:Prognosis; D016019:Survival Analysis; D014062:Tongue Neoplasms / Q000378:metabolism* / Q000473:pathology; D016159:Tumor Suppressor Protein p53 / Q000032:analysis
D006360:Heat-Shock Proteins; D016159:Tumor Suppressor Protein p53